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@ARTICLE{Rafiullah:181275,
author = {R. Rafiullah and A. B. Long and A. A. Ivanova and H. Ali
and S. Berkel and G. Mustafa and N. Paramasivam and M.
Schlesner$^*$ and S. Wiemann$^*$ and R. C. Wade and E.
Bolthauser and M. Blum and R. A. Kahn and T. Caspary and G.
A. Rappold},
title = {{A} novel homozygous {ARL}13{B} variant in patients with
{J}oubert syndrome impairs its guanine nucleotide-exchange
factor activity.},
journal = {European journal of human genetics},
volume = {25},
number = {12},
issn = {1018-4813},
address = {Basingstoke},
publisher = {Stockton Press},
reportid = {DKFZ-2022-01918},
pages = {1324 - 1334},
year = {2017},
note = {DKFZ-ZMBH Alliance},
abstract = {ARL13B encodes for the ADP-ribosylation factor-like 13B
GTPase, which is required for normal cilia structure and
Sonic hedgehog (Shh) signaling. Disruptions in cilia
structure or function lead to a class of human disorders
called ciliopathies. Joubert syndrome is characterized by a
wide spectrum of symptoms, including a variable degree of
intellectual disability, ataxia, and ocular abnormalities.
Here we report a novel homozygous missense variant
c.[223G>A] (p.(Gly75Arg) in the ARL13B gene, which was
identified by whole-exome sequencing of a trio from a
consanguineous family with multiple-affected individuals
suffering from intellectual disability, ataxia, ocular
defects, and epilepsy. The same variant was also identified
in a second family. We saw a striking difference in the
severity of ataxia between affected male and female
individuals in both families. Both ARL13B and
ARL13B-c.[223G>A] (p.(Gly75Arg) expression rescued the cilia
length and Shh defects displayed by Arl13b hennin (null)
cells, indicating that the variant did not disrupt either
ARL13B function. In contrast, ARL13B-c.[223G>A]
(p.(Gly75Arg) displayed a marked loss of ARL3 guanine
nucleotide-exchange factor activity, with retention of its
GTPase activities, highlighting the correlation between its
loss of function as an ARL3 guanine nucleotide-exchange
factor and Joubert syndrome.},
keywords = {ADP-Ribosylation Factors: genetics / ADP-Ribosylation
Factors: metabolism / Abnormalities, Multiple: diagnosis /
Abnormalities, Multiple: genetics / Adolescent / Adult /
Animals / Cell Line, Tumor / Cells, Cultured / Cerebellum:
abnormalities / Child / Eye Abnormalities: diagnosis / Eye
Abnormalities: genetics / Female / Guanosine Triphosphate:
metabolism / Homozygote / Humans / Kidney Diseases, Cystic:
diagnosis / Kidney Diseases, Cystic: genetics / Loss of
Function Mutation / Male / Mice / Mutation, Missense /
Pedigree / Retina: abnormalities / Guanosine Triphosphate
(NLM Chemicals) / ADP-Ribosylation Factors (NLM Chemicals) /
Arl13b protein, human (NLM Chemicals)},
cin = {B080 / W110},
ddc = {610},
cid = {I:(DE-He78)B080-20160331 / I:(DE-He78)W110-20160331},
pnm = {312 - Functional and structural genomics (POF3-312)},
pid = {G:(DE-HGF)POF3-312},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:29255182},
pmc = {pmc:PMC5865152},
doi = {10.1038/s41431-017-0031-0},
url = {https://inrepo02.dkfz.de/record/181275},
}